| Range |
~50 residues
|
| Organism |
Mitochondria |
| Reference |
Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6673 right column 2nd paragraphPubMed ID24901537
|
| Primary Source |
[267] Cheng EH et al., Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 1997 Dec 12 278(5345):1966-8 [268] Youle RJ, Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol. 2008 Jan9(1):47-59 DOI: 10.1038/nrm2308PubMed ID9395403, 18097445
|
| Comments |
P.6673 right column 2nd paragraph: "Proteolytic Processing: Disordered proteins particularly amenable to functional and site-specific processing events, such as targeted proteolysis. While some of these cleavage reactions produce toxic fragments, including aggregation prone species (see section 4), others result in modified proteins with novel functions. Proteolytic processing of the Bcl-2 family of proteins is one example. These proteins contain extended (∼50 residues) disordered loop regions that control pro- and antiapoptotic cellular responses (primary sources)." Primary source [267] p. 1966 left column top paragraph: "Bcl-2 is an integral intracellular membrane protein that inhibits programmed cell death induced by multiple insults in a wide variety of cell types (ref 1 therein)." Primary source [268] p.47 left column top paragraph: "The BCL-2 (B-cell lymphoma-2) gene was discovered at the t(14,18) chromosome translocation breakpoint in B-cell follicular lymphomas, where its transcription becomes excessively driven by the immunoglobulin heavy chain gene promoter and enhancer on chromosome 14 (Refs 1–3 therein)." |
| Entered by |
Uri M |
| ID |
116237 |